Aminodeoxychorismate synthase
| 4-amino-4-deoxychorismate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.85 | ||||||||
| CAS no. | 132264-37-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aminodeoxychorismate synthase (EC 2.6.1.85) is an enzyme that catalyzes the chemical reaction
- chorismate + L-glutamine 4-amino-4-deoxychorismate + L-glutamate
Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its two products are 4-amino-4-deoxychorismate and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is chorismate:L-glutamine amido-ligase. Other names in common use include ADC synthase, 4-amino-4-deoxychorismate synthase, and PabB. This enzyme participates in folate biosynthesis.
References
- Ye QZ, Liu J, Walsh CT (1990). "p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase". Proc. Natl. Acad. Sci. U.S.A. 87 (23): 9391–5. doi:10.1073/pnas.87.23.9391. PMC 55171. PMID 2251281.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Viswanathan VK, Green JM, Nichols BP (1995). "Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli". J. Bacteriol. 177 (20): 5918–23. PMC 177419. PMID 7592344.
{{cite journal}}: CS1 maint: multiple names: authors list (link)